ID A0A261G7X7_9BIFI Unreviewed; 399 AA.
AC A0A261G7X7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=BE0216_10885 {ECO:0000313|EMBL:QOL32886.1}, BEUL_1394
GN {ECO:0000313|EMBL:OZG67303.1};
OS Bifidobacterium eulemuris.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1765219 {ECO:0000313|EMBL:OZG67303.1, ECO:0000313|Proteomes:UP000216057};
RN [1] {ECO:0000313|EMBL:OZG67303.1, ECO:0000313|Proteomes:UP000216057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100216 {ECO:0000313|EMBL:OZG67303.1,
RC ECO:0000313|Proteomes:UP000216057};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
RN [2] {ECO:0000313|EMBL:QOL32886.1, ECO:0000313|Proteomes:UP000593943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100216 {ECO:0000313|EMBL:QOL32886.1,
RC ECO:0000313|Proteomes:UP000593943};
RA Kim J.;
RT "Genome sequencing of Bifidobacterium eulemuris_DSMZ_100216.";
RL Submitted (OCT-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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DR EMBL; MWWZ01000008; OZG67303.1; -; Genomic_DNA.
DR EMBL; CP062938; QOL32886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261G7X7; -.
DR KEGG; beu:BE0216_10885; -.
DR OrthoDB; 9763453at2; -.
DR Proteomes; UP000216057; Unassembled WGS sequence.
DR Proteomes; UP000593943; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42832:SF3; LL-DIAMINOPIMELATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:OZG67303.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000481}.
FT DOMAIN 37..386
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 399 AA; 43195 MW; 5BF84A4218CA5FB7 CRC64;
MRYDSPVRFS AVARSIPSNV FADMDRKVAA AIAEGHDVID LAKGNPDAYP AEFIREEAKK
AADDPANARY TPFDGKPAFL EAAAGWYARV HDVPLDCRSQ LFAVEGAVDG LAGLFSILVD
PGDAVAFVDP YYPSYHCMSV MAGAEEVLLP ALADRGFLPD LDAVPQKVWE RVKVLVLNYP
NNPTGAQAPR DFLRHAVDLA RRHRFVIVQD FAYAGLGVHG QQSSILAVPG AFDVAVEVCS
LSKMYAMAGW RAGFVAGNDD IVAHFKRYHY QMGSMISSIV QDAGAAALNS DQRCVDELAE
RYARRRGIVS RGLHDAGLDV FDSQGGIYVW ARTPAGYDGV GFADLVLKRA HVAVLPGSCF
GSVGADYVRF SLLKSDGELD EAVRRVADVL ARAANLNRP
//
